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4R4Y

Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria

Functional Information from GO Data
ChainGOidnamespacecontents
A0003948molecular_functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0042597cellular_componentperiplasmic space
B0003948molecular_functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B0042597cellular_componentperiplasmic space
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SD4 A 301
ChainResidue
AHIS150
AHOH436
AHOH437
AASP151
ATHR152
AASP172
AARG180
AASP183
ATHR203
AGLY204
AGLY206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10490104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17157318","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20800597","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9685368","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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